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  The structure of the Aquifex aeolicus MATE family multidrug resistance transporter and sequence comparisons suggest the existence of a new subfamily

Zhao, J., Xie, H., Mehdipour, A. R., Safarian, S., Ermler, U., Münke, C., et al. (2021). The structure of the Aquifex aeolicus MATE family multidrug resistance transporter and sequence comparisons suggest the existence of a new subfamily. Proceedings of the National Academy of Sciences of the United States of America, 118(46): e2107335118. doi:10.1073/pnas.2107335118.

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 Creators:
Zhao, Jiangfeng1, 2, Author              
Xie, Hao1, Author              
Mehdipour, Ahmad Reza3, Author              
Safarian, Schara1, Author              
Ermler, Ulrich1, Author              
Münke, Cornelia1, Author              
Thielmann, Yvonne1, Author              
Hummer, Gerhard3, Author              
Ebersberger, Ingo4, 5, 6, Author
Wang, Jingkang2, Author
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2State Key Laboratory for Chemical Engineering, Collaborative Innovation Center of Chemical Science and Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, 300072 Tianjin, P. R. China, ou_persistent22              
3Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
4Department for Applied Bioinformatics, Institute for Cell Biology and Neuroscience, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany, ou_persistent22              
5Senckenberg Biodiversity and Climate Research Centre Frankfurt (BIK-F), 60325 Frankfurt am Main, Germany, ou_persistent22              
6LOEWE Centre for Translational Biodiversity Genomics, 60325 Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: membrane protein structure; multidrug resistance transporter; phylogenetic analysis
 Abstract: Multidrug and toxic compound extrusion (MATE) transporters are widespread in all domains of life. Bacterial MATE transporters confer multidrug resistance by utilizing an electrochemical gradient of H+ or Na+ to export xenobiotics across the membrane. Despite the availability of X-ray structures of several MATE transporters, a detailed understanding of the transport mechanism has remained elusive. Here we report the crystal structure of a MATE transporter from Aquifex aeolicus at 2.0-Å resolution. In light of its phylogenetic placement outside of the diversity of hitherto-described MATE transporters and the lack of conserved acidic residues, this protein may represent a subfamily of prokaryotic MATE transporters, which was proven by phylogenetic analysis. Furthermore, the crystal structure and substrate docking results indicate that the substrate binding site is located in the N bundle. The importance of residues surrounding this binding site was demonstrated by structure-based site-directed mutagenesis. We suggest that Aq_128 is functionally similar but structurally diverse from DinF subfamily transporters. Our results provide structural insights into the MATE transporter, which further advances our global understanding of this important transporter family.

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Language(s): eng - English
 Dates: 2021-04-192021-10-052021-11-092021-11-16
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.2107335118
PMID: 34753818
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 118 (46) Sequence Number: e2107335118 Start / End Page: - Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230